SitesBLAST

T69 (= T70) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
D258 (≠ E236) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
T262 (= T240) binding Na(+); mutation to A: Alters bicarbonate transport.
G300 (≠ A278) binding Na(+)
A301 (≠ M279) binding hydrogencarbonate
T302 (≠ I280) binding Na(+); mutation to A: Alters bicarbonate transport.
A471 (≠ K431) mutation to N: Alters bicarbonate transport.
L476 (= L436) mutation to S: Alters bicarbonate transport.
A486 (≠ S446) mutation to E: Alters bicarbonate transport.
L490 (= L450) mutation to Q: Alters bicarbonate transport.

6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
27% identity, 71% coverage: 10:362/496 of query aligns to 8:383/392 of 6ki1B

query
sites
6ki1B

F

F

S

R

N

N

I

L

R

Q

G

G

D

D

V

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L

F

A

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G

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A

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A

A

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C

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I

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K

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N

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C

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A
x
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V

binding bicarbonate ion: T68 (= T70), A300 (≠ M279)
binding sodium ion: D257 (≠ E236), T261 (= T240), G299 (≠ A278), A300 (≠ M279), T301 (≠ I280)

7v74A Thermostabilized human prestin in complex with sulfate (see paper)
24% identity, 96% coverage: 8:485/496 of query aligns to 21:570/597 of 7v74A

query
sites
7v74A

E

E

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D

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D

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A

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D

D

D

binding cholesterol: L206 (vs. gap), K209 (vs. gap), V379 (≠ M329)
binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: V176 (≠ G153), F388 (≠ W337), F414 (≠ V362)
binding sulfate ion: F80 (≠ I66), V286 (≠ E236), S329 (≠ M279), F330 (≠ I280)

7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
24% identity, 91% coverage: 8:460/496 of query aligns to 21:523/575 of 7lhvA

query
sites
7lhvA

E

R

W

W

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Y

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x
A

A

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N

L

A

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L

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L

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L

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N

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x
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F

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A

C

A

A

L

L

V

A

A

A

V

I

M

V

I

I

M

S

V

A

S

V

I

S

G

G

T

L

F

V

S

D

W

Y

S

D

S

E

I

A

T

I

N

F

L

L

-

W

K

R

K

V

H

D

P

K

L

R

S

D

T

F

N

S

I

L

V

W

M

T

V

I

T

T

T

S

V

T

V

I

I

T

V

L

V

F

W

F

T

-

H

-

N

G

L

I

A
x
E

L

I

G

G

V

V

F
x
L

V

V

G

G

V

V

L
x
G

L

F

A

S

T

L

L
x
A

F

F

F

V

A

I

N

H

K

E

-

S

-

A

-

N

-

P

-

H

-

I

-

A

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V

I

L

G

G

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R

F

L

M

P

I

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K

T

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Y

Q

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N

G

I

D

K

Q

Q

S

Y

V

P

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A

Y

Y

-

T

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Y

-

N

-

G

-

I

-

V

-

I

-

V

R

R

V

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I

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G

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Q

P

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Y

F

F

A

A

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N

S

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F

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K

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L

-

R

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Y

K

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A

A

V

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D

K

K

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Y

V

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N

-

R

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G

-

L

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I

V

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D

L

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I

N

N

A

F

H

V

F

I

W

L

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E

I

M

T

S

S

P

V

V

S

T

S

H

L

I

D

D

K

S

V

S

V

A

I

V

K

E

F

A

R

L

R

K

E

E

binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ I106), R127 (≠ K107), W130 (≠ S110)
binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L108), L131 (= L111), E409 (≠ A368), L413 (≠ F372), G417 (≠ L376), A421 (≠ L380)
binding sulfate ion: A84 (≠ G71), S321 (≠ M279), F322 (≠ I280)

7v75A Thermostabilized human prestin in complex with salicylate (see paper)
23% identity, 97% coverage: 7:485/496 of query aligns to 11:578/605 of 7v75A

query
sites
7v75A

M

L

E

E

W

W

F

L

S

P

-

K

-

Y

N

N

I

L

R

K

-

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W

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L

G

G

D

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V

L

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G

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L

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-

Y

-

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-

L

-

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D

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K

R

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G

V

V

G

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M

V

G

G

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K

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L

L

P

P

I

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F

-

L

-

W

-

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P

D

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V

V

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-

N

D

L

L

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L

L

F

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L

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L

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G

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I

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I

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G

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L

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M

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M

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A

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L

K

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Q

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N

N

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Q

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K

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G

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G

G

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M

N

N

I

I

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V

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G

G

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F

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C

M

Y

A

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G

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M

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F

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N

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V

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M

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A

A

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M

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I

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x
V

V

N

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G

G

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M

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x
F

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M

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F

W

L

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L

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A

G

L

L

G

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V

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V

V

G

G

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L

S

L

L

A

L

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T

L

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F

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N

T

K

Q

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G

G

R

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I

-

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-

G

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F

Y

M

R

I

D

V

V

K

K

A

Q

E

Y

Q

P

S

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G

A

D

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Q

E

-

V

-

P

S

G

V

V

R

K

T

I

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F

R

R

V

I

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D

G

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Q

P

V

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F

Y

F

F

A

A

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N

S

S

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A

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F

F

V

K

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F

L

D

K

F

R

K

K

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T

A

G

V

V

D

D

K

P

V

V

-

K

-

V

-

L

-

A

-

R

-

K

-

A

-

L

-

K

-

I

-

E

-

K

-

E

-

I

-

K

-

P

-

K

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V

-

D

-

F

-

H

-

T

-

L

V

I

I

L

D

D

L

F

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S

N

A

A

V

H

S

F

F

W

V

D

D

I

T

T

V

S

G

V

V

S

K

S

T

L

L

D

K

K

E

V

I

V

V

I

K

K

E

F

Y

R

R

R

E

E

I

G

G

A

V

D

Q

V

V

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Y

L

L

V

A

G

G

M

C

N

N

A

A

A

S

T

V

E

V

T

E

V

K

V

L

D

E

K

R

F

G

A

G

V

F

H

F

N

D

D

D

binding cholesterol: L206 (vs. gap), V379 (≠ M329)
binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F388 (≠ W337), F414 (≠ V362)

D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
25% identity, 65% coverage: 15:335/496 of query aligns to 82:452/741 of D7PC76

query
sites
D7PC76

G

G

D

D

V

I

L

V

A

S

G

G

I

I

V

S

V

T

A

G

L

V

A

L

L

Q

I

L

P

P

E

Q

A

G

I

L

A

A

F

F

S

A

I

M

I

L

A

A

G

A

V

V

D

P

P

P

K

V

V

F

G

G

L

L

Y

Y

A

S

S

S

F

F

C

Y

I

P

A

V

V

I

V

M

I

Y

A

C

F

F

V

F

G

G

-

T

-

S

-

R

-

H

-

I

-

S

-

I

G

G

R

P

P

F

G

A

M

V

I

I

S

S

A

L

A

M

T

I

G

G

A

G

M

V

A

A

L

V

L

R

M

L

V

V

-

P

-

D

-

I

-

V

-

I

-

P

-

G

-

V

-

N

-

A

-

T

-

N

-

S

T

T

L

E

V

A

K

R

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D

H

A

-

L

G

R

L

V

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K

Y

V

L

A

L

M

A

S

A

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T

T

L

L

T

T

G

G

V

I

I

I

Q

Q

I

F

I

C

A

L

G

G

Y

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I

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K

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G

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F

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V

L

V

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G

G

F

F

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N

T

A

A

L

A

A

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L

H

I

V

F

F

M

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A

S

Q

M

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K

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Y

L

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N

G

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M

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N

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G

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K

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W

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N

N

L

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D

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L

S

L

L

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F

I

H

L

L

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V

Y

Y

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S

A

I

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A

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A

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G

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F

L

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V

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M

I

M

S

T

M

A

A

A

K

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D

A

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N

L

K

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D

G

T

Y

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Q

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V

D

D

R

G

N

N

R

Q

E

E

C

L

K

I

G

A

Q

L

G

G

I

L

A

C

N

N

I

S

G

T

S

G

G

S

L

L

L

F

G

Q

G

T

M

F

A

A

G

I

C

S

A

C

M

S

I

L

G
x
S

Q

R

S

S

I

L

I

V

N

Q

V

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K

G

S

T

G

G

R

K

G

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L

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G

F

C

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A

A

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L

L

M

L

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L

L

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L

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V

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V

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A

L

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G

G

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W

L

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F

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P

P

M

Q

A

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L

L

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A

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M

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M

V

V

N

S

L

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G

G

T

M

F

F

GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
S398 (≠ G281) binding salicylate

Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 80% coverage: 15:411/496 of query aligns to 82:514/744 of Q9JKQ2

query
sites
Q9JKQ2

G

G

D

D

V

L

L

V

A

S

G

G

I

I

V

S

V

T

A

G

L

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A

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G

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M

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I

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x
I

-
x
P

-
x
G

L
x
V

V
x
N

K
x
A

E
x
T

H
x
N

G
|
G

L
x
T

E

E

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A

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D

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A

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L

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V

V

I

F

G

G

-

L

-

G

-

K

-

E

-

F

-

N

-

E

-

R

-

F

-

K

K

E

T

K

L

L

P

P

S

A

P

P

L

-

V

-

C

-

I

-

V

I

V

P

L

L

T

E

A

F

F

F

A

A

M

V

I

V

V

M

G

G

I

T

D

G

I

I

R

S

T

A

V

G

G

F

D

N

M

L

G

H

E

E

-

S

-

Y

-

S

-

V

-

D

L

V

P

V

D

G

T

T

L

L

P

P

I

L

F

G

L

L

W

L

P

P

D

-

V

-

P

P

L

A

N

N

L

P

D

D

T

T

L

S

L

L

I

F

I

H

L

L

P

V

Y

Y

-

V

-

D

S

A

I

I

G

A

L

I

A

A

V

I

V

V

G

G

L

F

L

S

E

V

S

T

M

I

M

S

T

M

A

A

A

K

I

T

V

L

D

A

D

N

L

K

T

H

D

G

T

Y

K

Q

S

V

D

D

R

G

N

N

R

Q

E

E

C

L

K

I

G

A

Q

L

G

G

I

I

A

C

N

N

I

S

G

I

S

G

G

S

L

L

L

F

G

Q

G

T

M

F

A

S

G

I

C

S

A

C

M

S

I

L

G
x
S

Q
x
R

S

S

I

L

I

V

N

Q

V

E

K

G

S

T

G

G

R

K

G

T

R

Q

L

L

S

A

T

G

F

C

I

L

A

A

G

S

T

L

L

M

L

I

L

L

I

L

M

V

V

I

V

L

F

A

L

T

G

G

E

F

W

L

I

F

K

E

Q

S

I

L

P

P

M

Q

A

A

A

V

L

L

V

S

A

A

V

I

M

V

I

I

M

V

V

N

S

L

I

K

G

G

T

M

F

F

S

-

W

-

S

M

S

Q

I

F

T

S

N

D

L

L

K

P

K

F

H

F

P

W

L

R

S

T

T

S

N

K

I

I

V

E

M

L

V

-

T

-

T

T

V

I

V

W

I

L

V

T

W

F

T

V

H

S

N

S

L

L

A

F

L

L

G

G

V

L

F

D

V

Y

G

G

V

L

L

I

L

T

A

A

T

V

L

I

F

-

A

-

N

-

K

-

I

I

G

A

R

L

F

L

M

T

I

V

V

I

K

Y

A

R

E

T

Q

Q

S

S

G

-

D

-

Q

-

S

-

V

-

R

P

T

S

Y

Y

R

K

V

V

I

L

G

G

Q

Q

V

L

158:168 (vs. 80:86, 9% identical) Involved in motor function
S398 (≠ G281) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
R399 (≠ Q282) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.

7lguA Structure of human prestin in the presence of nacl (see paper)
25% identity, 65% coverage: 15:335/496 of query aligns to 70:440/680 of 7lguA

query
sites
7lguA

G

G

D

D

V

L

L

V

A

S

G

G

I

I

V

S

V

T

A

G

L

V

A

L

L

Q

I

L

P

P

E

Q

A

G

I

L

A

A

F

F

S

A

I

M

I

L

A

A

G

A

V

V

D

P

P

P

K

I

V

F

G

G

L

L

Y

Y

A

S

S

S

F

F

C

Y

I

P

A

V

V

I

V

M

I

Y

A

C

F

F

V

L

G

G

-

T

-

S

-

R

-

H

-

I

-

S

-

I

G

G

R

P

P

F

G

A

M

V

I

I

S

S

A

L

A

M

T

I

G

G

A

G

M

V

A

A

L

V

L

R

M

L

V

V

T

P

-

D

-

I

-

V

-

I

-

P

-

G

L

V

V

N

K

A

E

T

H

N

G

G

L

T

E

E

-

A

-

R

-

D

-

A

-

L

-

R

-

V

-

K

Y

V

L

A

L

M

A

S

A

V

T

T

L

L

T

S

G

G

V

I

I

I

Q

Q

I

F

I

C

A

L

G

G

Y

V

I

C

K

R

L

F

G

G

S

F

L

V

M

A

R

I

F

Y

V

L

S

T

R

E

S

P

V

L

V

V

T

R

G

G

F

F

V

T

N

T

A

A

L

A

A

A

I

V

L

H

I

V

F

F

M

T

A

S

Q

M

L

L

P

K

E

Y

L

L

T

F

N

G

V

V

T

K

W

T

H

K

V

R

Y

Y

A

S

-

G

-
x
I

-

F

-

S

-

V

-

Y

-

S

-

T

-

V

-

A

-

V

-

L

-

Q

-

N

-

V

-

K

-

N

M

L

T

N

A

V

A

C

G

S

L

L

G

G

I

V

I

G

Y

L

L

M

F

V

P

F

Y

G

L

L

P

L

V

L

I

G

G

G

K

K

-

E

-

F

-

N

-

E

-

R

-

F

-

K

-

E

T

K

L

L

P

P

S

A

P

P

L

-

V

-

C

-

I

-

V

I

V

P

L

L

T

E

A

F

F

F

A

A

M

V

I

V

V

M

G

G

I

T

D

G

I

I

R

S

T

A

V

G

G

F

D

N

M

L

G

K

E

E

L

S

P

Y

D

N

-

V

-

D

-

V

-

G

T

T

L

L

P

P

I

L

F

G

L

L

W

L

P

P

D

-

V

-

P

P

L

A

N

N

L

P

D

D

T

T

L

S

L

L

I

F

I

H

L

L

P

V

Y

Y

-

V

-

D

S

A

I

I

G

A

L

I

A

A

V

I

V

V

G

G

L

F

L

S

E

V

S

T

M

I

M

S

T

M

A

A

A

K

I

T

V

L

D

A

D

N

L

K

T

H

D

G

T

Y

K

Q

S

V

D

D

R

G

N

N

R

Q

E

E

C

L

K

I

G

A

Q

L

G

G

I

L

A

C

N

N

I

S

G

I

S

G

G

S

L

L

L

F

G

Q

G

T

M

F

A

S

G

I

C

S

A

C

M

S

I

L

G

S

Q

R

S

S

I

L

I

V

N

Q

V

E

K

G

S

T

G

G

R

K

G

T

R

Q

L

L

S

A

T

G

F

C

I

L

A

A

G

S

T

L

L

M

L

I

L

L

I

L

M

V

V

I

V

L

F

A

L

T

G

G

E

F

W

L

I

F

K

E

Q

S

I

L

P

P

M

Q

A

A

A

V

L

L

V

S

A

A

V

I

M

V

I

I

M

V

V

N

S

L

I

K

G

G

T

M

F

F

binding cholesterol: I228 (vs. gap)

Sites not aligning to the query:

binding cholesterol: 474, 478, 481, 482

Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
25% identity, 65% coverage: 15:335/496 of query aligns to 82:452/744 of Q9EPH0

query
sites
Q9EPH0

G

G

D

D

V

L

L

V

A

S

G

G

I

I

V

S

V

T

A

G

L

V

A

L

L

Q

I

L

P

P

E

Q

A

G

I

L

A

A

F

F

S

A

I

M

I
x
L

A

A

G

A

V

V

D

P

P

P

K

V

V

F

G

G

L

L

Y

Y

A

S

S

S

F

F

C

Y

I

P

A

V

V

I

V

M

I

Y

A

C

F

F

V

F

G

G

-

T

-

S

-

R

-

H

-

I

-

S

-

I

G

G

R

P

P

F

G

A

M

V

I

I

S

S

A

L

A

M

T

I

G

G

A

G

M

V

A

A

L
x
V

L

R

M

L

V

V

T

P

-
x
D

-

I

-

V

-

I

-

P

-

G

L

V

V

N

K

A

E

T

H

N

G

G

L

T

E
|
E

-

A

-

R

-

D

-

A

-

L

-

R

-

V

-
x
K

Y

V

L

A

L

M

A

S

A

V

T

T

L

L

T

S

G

G

V

I

I

I

Q

Q

I

F

I

C

A

L

G

G

Y

V

I

C

K
x
R

L

F

G

G

S

F

L

V

M
x
A

R

I

F

Y

V

L

S

T

R

E

S

P

V

L

V

V

T

R

G

G

F

F

V

T

N

T

A

A

L

A

A

A

I

V

L

H

I

V

F

F

M

T

A

S

Q

M

L

L

P

K

E

Y

L

L

T

F

N

G

V

V

T
x
K

W

T

H
x
K

V
x
R

Y

Y

A

S

-

G

-

I

-

F

-

S

-

V

-

Y

-

S

-

T

-

V

-

A

-

V

-

L

M

Q

T

N

A

V

A

K

G

N

L

L

G

N

I

V

I

C

Y

S

L

L

F

G

P

V

Y

G

L

L

P

M

V

V

I

F

G

G

-

L

-

G

-
x
K

-
x
E

-

F

-

N

-

E

-
x
R

-

F

-
x
K

K

E

T
x
K

L

L

P

P

S

A

P

P

L

-

V

-

C

-

I

-

V

I

V

P

L

L

T

E

A

F

F

F

A

A

M

V

I

V

V

M

G

G

I

T

D

G

I

I

R

S

T

A

V

G

G

F

D

N

M

L

G

H

E

E

-

S

-

Y

-

S

-

V

-

D

L

V

P

V

D

G

T

T

L

L

P

P

I

L

F

G

L

L

W

L

P

P

D

-

V

-

P

P

L

A

N

N

L
x
P

D
|
D

T

T

L

S

L

L

I

F

I

H

L

L

P

V

Y

Y

-

V

-
x
D

S

A

I

I

G

A

L

I

A

A

V

I

V

V

G

G

L

F

L

S

E

V

S

T

M

I

M

S

T

M

A

A

A
x
K

I

T

V

L

D

A

D

N

L

K

T

H

D

G

T

Y

K

Q

S

V

D

D

R

G

N

N

R

Q

E

E

C

L

K

I

G

A

Q

L

G

G

I

I

A

C

N

N

I

S

G

I

S

G

G

S

L

L

L

F

G
x
Q

G

T

M

F

A

S

G

I

C

S

A

C

M

S

I

L

G
x
S

Q
x
R

S

S

I

L

I

V

N

Q

V

E

K

G

S

T

G

G

G
|
G

R
x
K

G

T

R

Q

L

L

S

A

T

G

F

C

I

L

A

A

G

S

T

L

L

M

L

I

L

L

I

L

M

V

V

I

V

L

F

A

L

T

G

G

E

F

W
x
L

I

F

K

E

Q

S

I

L

P

P

M

Q

A

A

A

V

L

L

V

S

A

A

V

I

M

V

I

I

M

V

V

N

S

L

I

K

G

G

T

M

F

F

L104 (≠ I37) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
V149 (≠ L75) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
D154 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
D155 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
E169 (= E87) mutation to Q: No effect.
K177 (vs. gap) mutation to Q: No effect.
R197 (≠ K107) mutation to Q: Shifts the voltage-sensitivity to more negative values.
A202 (≠ M112) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
K233 (≠ T143) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
K235 (≠ H145) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
R236 (≠ V146) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.; mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235.
K276 (vs. gap) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
E277 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
R281 (vs. gap) mutation to Q: No effect; when associated with Q-283 and Q-285.
K283 (vs. gap) mutation to Q: No effect; when associated with Q-218 and Q-285.
K285 (≠ T169) mutation to Q: No effect; when associated with Q-281 and Q-283.
P331 (≠ L216) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
D332 (= D217) mutation to Q: No effect.
D342 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more positive values.
K359 (≠ A242) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
Q389 (≠ G272) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
S398 (≠ G281) Controls the electromotile activity; mutation to C: Does not affect anion-dependent electromotility-related charge movement. Strongly attenuates inhibition by oxalate of electromotility-related charge movement. Is sensible to intracellular thiol-reactive reagents. Is completely insensitive to both reagents applied to the extracellular face of the membrane. Strongly affects the interaction with oxalate.
R399 (≠ Q282) Contributes to anion binding; mutation to C: Largely abolishes anion-dependent electromotility-related charge movement.; mutation to E: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to K: Does not affect anion-dependent electromotility-related charge movement.; mutation to Q: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to S: Does not affect anion-dependent electromotility-related charge movement. Abrogates salicylate inhibition of electromotility-related charge movement.
G408 (= G291) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
K409 (≠ R292) mutation to Q: No effect.
L431 (≠ W314) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.

Sites not aligning to the query:

465 S→C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
485 D→C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
505:718 Extended region for STAS domain
557 K→Q: No effect; when associated with Q-558 and Q-559.
558 R→Q: No effect; when associated with Q-557 and Q-559.
559 K→Q: No effect; when associated with Q-557 and Q-558.
571 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
572 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
577 K→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.

P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
25% identity, 65% coverage: 15:335/496 of query aligns to 82:452/744 of P58743

query
sites
P58743

G

G

D

D

V

L

L

V

A

S

G

G

I

I

V

S

V

T

A

G

L

V

A

L

L

Q

I

L

P

P

E

Q

A

G

I

L

A

A

F
|
F

S

A

I

M

I

L

A

A

G

A

V

V

D

P

P

P

K

I

V

F

G

G

L

L

Y

Y

A

S

S

S

F

F

C

Y

I

P

A

V

V

I

V

M

I

Y

A

C

F

F

V

L

G

G

-

T

-

S

-

R

-

H

-

I

-

S

-

I

G

G

R

P

P

F

G

A

M

V

I

I

S

S

A

L

A

M

T

I

G

G

A

G

M

V

A

A

L

V

L

R

M

L

V

V

T

P

-

D

-

I

-

V

-

I

-

P

-

G

L

V

V

N

K

A

E

T

H

N

G

G

L

T

E

E

-

A

-

R

-

D

-

A

-

L

-

R

-

V

-

K

Y

V

L

A

L

M

A

S

A

V

T

T

L

L

T

S

G

G

V

I

I

I

Q

Q

I

F

I

C

A

L

G

G

Y

V

I

C

K

R

L

F